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Tika Hairani
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Annales Bogorienses
Published by Badan Riset dan Inovasi Nasional
ISSN : 05178452     EISSN : 24077518     DOI : https://doi.org/10.55981/ann.bogor
Core Subject :
Annales Bogorienses aims to disseminate high-quality scientific research in the field of life sciences, with a strong emphasis on advancing knowledge and applications in biotechnology, molecular biology, biochemistry, bioinformatics, and bioengineering. The journal serves as a platform for researchers, academicians, and practitioners to share original findings, innovative methodologies, and critical reviews that contribute to scientific progress and sustainable development. The journal covers research in biotechnology, molecular biology, biochemistry, bioinformatics, and bioengineering. It publishes original research articles, reviews, and short communications, and is committed to rigorous peer review and open access for the widest possible dissemination of scientific knowledge.
Arjuna Subject : -
Articles 203 Documents
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Overproduction and Purification of Soluble Recombinant Human Granulocyte Colony Stimulating Factor in Escherichia coli Using Thioredoxin as Fusion Dian Fitria Agustiyanti; Debbie Sofie Retnoningrum; Heni Rachmawati; Asrul Muhamad Fuad
Annales Bogorienses Vol. 21 No. 1 (2017): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2017.v21.n1.1-8

Abstract

Recombinant human Granulocyte Colony Stimulating Factor (G-CSF) has been produced in a soluble form in Escherichia coli BL21 (DE3) as a fusion protein. The open reading frame of G-CSF was synthetically constructed in previous work and was codon optimized for best expression in E. coli. In this research, the gene was fused to thioredoxin (Trx) at the N-terminal in pET32 vector. The purpose of this research was to optimize the overproduction and purification processes to obtain high yield recombinant protein in soluble form, and to characterize the Trx-G-CSF fusion protein. Overproduction was performed using IPTG induction method for 3 and 6 hours. The protein was purified by Ni-NTA affinity chromatography and separated using gradient concentration of imidazole. The purified protein was then characterized by SDS-PAGE and Western Blot analysis. Further, enterokinase was used to separate G-CSF from the fusion protein. The purified form of G-CSF was subsequently characterized using Western Blot and mass spectrometry using MALDI-TOF. The results showed that the fusion protein was successfully produced in soluble part as much as 48.25% were obtained after 3 hours of induction. The yield of fusion protein was 67.37% from total protein (229.65 mg protein/L culture). The Western Blot analysis showed the G-CSF band at around 18.6 kDa. Mass spectrometry with MALDI-TOF/ TOF revealed that 25.86% of amino acid residue was recognized as part of human G-CSF sequence.
Enterococcus faecium 1.15 Isolated from Bakasam Showed Milk Clotting Activity Wendry Setiyadi Putranto; Kusmajadi Suradi; Hartati Chairunnisa; Apon Zaenal Mustopa; Harsi Dewantari Kusumaningrum; Maggy Thenawidjaja Suhartono
Annales Bogorienses Vol. 21 No. 1 (2017): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2017.v21.n1.9-14

Abstract

Rennin-like protease of many microorganisms behave similarly to chymosin and are potential alternatives of rennet. The lactic acid bacteria with milk clotting activity were isolated from Bakasam, an Indonesian traditional fermented meat. Screening assay was carried out using modified method of skim milk agar and milk clotting activity test, and the isolate was then identified using 16S rRNA. We found 4 isolates that showed MCA of 18-20 SU/mL. Identification using 16S rRNA indicated that the isolate ALG.1.15 was 99% identical with Enterococcus faecium. The isolate potentially produced renin-like protease to subtitute renin from veal.
Sequential Adaptation in Mammalian CHO-K1 Cells Producing Human Erythropoietin Popi Hadi Wisnuwardani; Endah Puji Septisetyani; Adi Santoso
Annales Bogorienses Vol. 21 No. 1 (2017): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2017.v21.n1.15-20

Abstract

The production of recombinant proteins for clinical applications using mammalian cell technology has become a prevalent system because of its capacity in assembling functional proteins. One of the main problems with CHO-K1 cells is that this cell has to grow in the presence of serum. However, the presence of serum will complicate the downstream step for protein production. Thus, protein produced in media without serum, theoretically, would be easier to purify. Technically, this type of cell can be produced by growing the CHO-K1 cells in serum-free media by using adaptation method in suspension condition. This research showed that through sequential adaptation using conditioned media, the CHO-K1 cell line that produces the human erythropoietin gene (hEPO) was able to grow in suspension culture using serum-free media. Based on Western blot analysis, it showed that the protein (hEPO) was able to be expressed in suspension culture with molecular mass of about 47 kDa.
Glucoamylase Production by Aspergillus awamori KT-11 In Solid State Fermentation Using Cassava Peel as Substrate Urip Perwitasari; Nuryati Nuryati; Ruth Melliawati; Yopi Yopi
Annales Bogorienses Vol. 21 No. 1 (2017): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2017.v21.n1.21-28

Abstract

Cassava has long been known as one of the main staple food in Indonesia. Whereas the cassava peel contains starch of approximately 72%, it is still underrated as a carbohydrate source for fermentation.The utilization of cassava peel as a substrate in solid state fermentation potentially replaces rice as a carbon source leading to more cost-effective production. This study aims at producing glucoamylase by means of solid state fermentation using Aspergillus awamori KT-11 and cassava peel as substrate. The study demonstrated that medium composition and drying technique affected the production of glucoamylase. The highest glucoamylase activities were identified when cassava peel and mineral media was used in fermentation, compared to only cassava peel; the combination of cassava peel, mineral, and rice bran; rice media or a mixture of rice, mineral and rice bran. Freeze-dried glucoamylase, furthermore, exhibited higher specific activity in contrast to the oven-dried one, with 452 U/mL and 365 U/mL, respectively. In conclusion, cassava peel plus mineral is a better substrate for glucosamine production by A. awamori KT-11 in solid state fermentation. Besides, powdered glucoamylase had been demonstrated to be capable of hydrolyzing starch-based biomass.
Comparison of Gene Expression Between Two Types of Anti-EGFRvIII ScFv Antibodies Having Different Variable Domain Orders in Escherichia coli Kartika Sari Dewi; Asrul Muhamad Fuad
Annales Bogorienses Vol. 21 No. 1 (2017): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2017.v21.n1.29-37

Abstract

Several studies reported that the expression of various kinds of single-chain variable fragment (scFv) antibodies in Escherichia coli are significantly influenced by the order of their variable domains. To date, the effect of the order of variable domains in the expression of scFv antibodies against epidermal growth factor receptor variant III (EGFRvIII) has not been reported. This study aimed to compare the expression between VH-linker-VL and VL-linker-VH domain orders of the anti-EGFRvIII scFv antibodies in E. coli expression system. Recombinant plasmids inserted with DNA encoding scFv proteins were transformed into E. coli NiCo21 (DE3) competent cells and characterized by colony PCR. The expression of scFv proteins was done by using optimum concentration of inducer. Total proteins, soluble periplasmic and cytoplasmic proteins, also extracellular proteins were isolated, subsequently characterized by SDS-PAGE, Slot Blot, and ImageJ software analyses. The antigen-binding activity of both scFvs proteins against EGFRvIII was observed. The results showed that the relative percentage of scFv expression with VH-linker-VL domain order is higher than that of VL-linker-VH in each compartment. Moreover, both of scFvs proteins have antigen-binding activity against EGFRvIII.
EDITOR'S PREFACE Syamsidah Rachmawati
Annales Bogorienses Vol. 21 No. 1 (2017): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar

Abstract

EDITOR'S PREFACE Syamsidah Rachmawati
Annales Bogorienses Vol. 21 No. 2 (2017): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ab.v21i2.319

Abstract

EDITOR'S PREFACE Puspita Lisdiyanti
Annales Bogorienses Vol. 24 No. 2 (2020): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2020.v24.n2.%p

Abstract

EDITOR'S PREFACE Puspita Lisdiyanti
Annales Bogorienses Vol. 24 No. 1 (2020): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2020.v24.n1.%p

Abstract

EDITOR'S PREFACE Puspita Lisdiyanti
Annales Bogorienses Vol. 23 No. 2 (2019): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2019.v23.n2.%p

Abstract

Page 18 of 21 | Total Record : 203

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